2001
βIII Spectrin Binds to the Arp1 Subunit of Dynactin*
Holleran E, Ligon L, Tokito M, Stankewich M, Morrow J, Holzbaur E. βIII Spectrin Binds to the Arp1 Subunit of Dynactin*. Journal Of Biological Chemistry 2001, 276: 36598-36605. PMID: 11461920, DOI: 10.1074/jbc.m104838200.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBinding SitesBrainCell MembraneCOS CellsCytoplasmCytosolDynactin ComplexElectrophoresis, Polyacrylamide GelGlutathione TransferaseImmunoblottingImmunohistochemistryMicrofilament ProteinsMicrotubule-Associated ProteinsPrecipitin TestsProtein BindingProtein IsoformsProtein Structure, TertiaryRatsSpectrinSrc Homology DomainsTwo-Hybrid System TechniquesConceptsBetaIII spectrinGolgi vesicle traffickingMicrotubule motor complexAssociation of dyneinVesicle traffickingVesicular cargoRat brain cytosolMitotic spindleIntracellular motorsCytoplasmic dyneinCleavage furrowDynactinInterphase cellsArp1Spectrin isoformsCytoplasmic vesiclesF-actinActin bindsEndoplasmic reticulumPerinuclear regionNovel localizationSpectrinDyneinBrain cytosolΒIII spectrin
1993
The 270 kDa splice variant of erythrocyte beta-spectrin (beta I sigma 2) segregates in vivo and in vitro to specific domains of cerebellar neurons.
Malchiodi-Albedi F, Ceccarini M, Winkelmann J, Morrow J, Petrucci T. The 270 kDa splice variant of erythrocyte beta-spectrin (beta I sigma 2) segregates in vivo and in vitro to specific domains of cerebellar neurons. Journal Of Cell Science 1993, 106 ( Pt 1): 67-78. PMID: 8270644, DOI: 10.1242/jcs.106.1.67.Peer-Reviewed Original ResearchConceptsBeta IPostsynaptic densityMultiple alternative transcriptsBeta-spectrin isoformBeta-spectrin genePlasma membrane stainingAlpha beta heterodimersNon-erythroid alpha-spectrinRegion of alphaCerebellar granule cellsDistinct genesPrecise segregationSubstantial homologyBiochemical restrictionsSingle protein bandAlternative transcriptsDistinct cytoplasmicUnique sequencesCerebellar neuronsSpectrin isoformsBeta heterodimerAlpha-spectrinSpectrin complexSplice variantsTargeting mechanism
1989
Functional diversity among spectrin isoforms
Coleman T, Fishkind D, Mooseker M, Morrow J. Functional diversity among spectrin isoforms. Cytoskeleton 1989, 12: 225-247. PMID: 2655937, DOI: 10.1002/cm.970120405.Peer-Reviewed Original ResearchConceptsSpectrin isoformsBeta subunitMembrane skeletal proteinsFunctional diversityUbiquitous familySubcellular localizationMembrane linkageCommon alpha subunitSkeletal proteinsAlpha subunitNonerythroid spectrinStructural comparisonCell typesMajor functional differencesSpectrinFunctional differencesSubunitsIsoformsFunctional propertiesSummary of studiesProteinDiversityObserved differencesOwn laboratoryLinkage
1987
Characterization of intestinal brush border cytoskeletal proteins of normal and neoplastic human epithelial cells. A comparison with the avian brush border.
Carboni J, Howe C, West A, Barwick K, Mooseker M, Morrow J. Characterization of intestinal brush border cytoskeletal proteins of normal and neoplastic human epithelial cells. A comparison with the avian brush border. American Journal Of Pathology 1987, 129: 589-600. PMID: 3425692, PMCID: PMC1899811.Peer-Reviewed Original ResearchConceptsMicrovillar actin bundlesActin binding proteinsHuman brush borderIntestinal epithelial cell brush bordersEpithelial cell brush bordersBrush borderMicrovillar proteinsHuman epithelial cellsCytoskeletal matrixCytoskeletal proteinsMultiple proteinsActin bundlesImmunolocalization studiesSpectrin isoformsMammalian sourcesMajor proteinsDifferentiation stateBinding proteinProtein myosinProteinTerminal webCell brush borderCytoskeletonNeoplastic stateMature enterocytes